Fitzpatrick Institute for Photonics Fitzpatrick Institute for Photonics
Pratt School of Engineering
Duke University

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Eric J. Toone, Professor Emeritus of Chemistry

Eric J. Toone
Contact Info:
Office Location:  B120 LSRC
Office Phone:  (919) 681-5161, (919) 660-1506
Email Address: send me a message
Web Page:  http://www.chem.duke.edu/%7Etoone/labgroup/

Education:

Ph.D.University of Toronto (Canada)1988
M.S.University of Toronto (Canada)1985
B.S.University of Guelph (Canada)1983
Specialties:

Organic
Biomolecular Structure and Function
Synthesis
Research Interests:

Dr. Toone is a physical organic chemist who studies relationships between structure and activity in the context of biology. Currently active programs exist in biocatalysis/applied enzymology, ligand binding and the activity of water, and the synthesis of novel donors of nitric oxide. The study of these problems makes use of synthetic organic chemistry, traditional enzymology, isothermal titration microcalorimetry, and the techniques of directed evolution.

Keywords:

Acetamides • Acetylene • Acid-Base Equilibrium • Acrylates • Acrylic Resins • Administration, Inhalation • Administration, Topical • Adsorption • Aldehyde Oxidoreductases • Aldehyde-Lyases • Amidohydrolases • Amino Acid Sequence • Aminoglycosides • Animals • Animals, Newborn • Anti-Bacterial Agents • Antibodies, Monoclonal • Antibody Specificity • Antineoplastic Agents • Aorta • Apoenzymes • Asparagine • Autolysis • Azides • Bacteria • Bacterial Infections • Bacterial Proteins • Bacterial Secretion Systems • Bacterial Toxins • Base Sequence • beta Catenin • Binding Sites • Biochemistry • Biological Availability • Biological Transport, Active • Biopolymers • Biosensing Techniques • Biotransformation • Biphenyl Compounds • Bis-Trimethylammonium Compounds • Breast Neoplasms • Bridged Compounds • Buffers • Calcium • Calmodulin • Calorimetry • Caprylates • Carbohydrate Conformation • Carbohydrate Metabolism • Carbohydrate Sequence • Carbohydrates • Carbon • Carbonic Anhydrases • Carboxylic Acids • Catalysis • Catalytic Domain • Cations • Cations, Divalent • Cell Division • Cell Line • Cell Line, Tumor • Cell Membrane Permeability • Cell Physiological Processes • Cell Proliferation • Cell Transformation, Neoplastic • Chemistry • Chlamydia Infections • Chlamydia trachomatis • Choline • Chromatography, Affinity • Chromatography, High Pressure Liquid • Cinnamates • Circular Dichroism • Cloning, Molecular • Clostridium perfringens • Cobalt • Colonic Neoplasms • Combinatorial Chemistry Techniques • Computational Biology • Computer Simulation • Concanavalin A • Conjunctiva • Conjunctival Diseases • Consensus Sequence • Copper • Cornea • Cross Reactions • Crystallization • Crystallography, X-Ray • Cysteine • Cytidine Monophosphate N-Acetylneuraminic Acid • Cytidine Triphosphate • Developing Countries • Directed Molecular Evolution • Disaccharides • Disease • Disease Models, Animal • Disulfides • DNA • DNA, Bacterial • DNA, Single-Stranded • Dogs • Dose-Response Relationship, Drug • Drosophila melanogaster • Drug Combinations • Drug Design • Drug Discovery • Drug Evaluation, Preclinical • Drug Stability • Edetic Acid • Elasticity • Electrodes • Entropy • Enzyme Inhibitors • Enzyme-Linked Immunosorbent Assay • Enzymes • Enzymes, Immobilized • Epitopes • Escherichia coli • Escherichia coli Proteins • Ethacrynic Acid • Exodeoxyribonucleases • Factor XIIIa • Ferrous Compounds • Fourier Analysis • Galanthus • Galectin 3 • Gas Chromatography-Mass Spectrometry • Gene Expression Regulation, Bacterial • Gene Library • Genes, Bacterial • Genes, Regulator • Genes, Reporter • Genetic Engineering • Genetic Therapy • Germanium • Gluconates • Glucosides • Glutamic Acid • Glutamine • Glycolipids • Glycopeptides • Glycosides • Glycosylation • Guanosine Triphosphate • HeLa Cells • Hemagglutination • Hemagglutination Tests • High-Throughput Screening Assays • Histidine • Histone Demethylases • Holoenzymes • Humans • Hyaluronic Acid • Hydro-Lyases • Hydrogen • Hydrogen Bonding • Hydrogen-Ion Concentration • Hydrolysis • Hydrolyzable Tannins • Hydrophobic and Hydrophilic Interactions • Hydroxamic Acids • Hyperemia • Hypertension, Pulmonary • Imidazoles • Immobilized Proteins • Immunoglobulin G • Immunoglobulin kappa-Chains • Immunoglobulin M • Inclusion Bodies • Indicators and Reagents • Intraocular Pressure • Iron Chelating Agents • Kinetics • Lactones • Lactose • Lectins • Ligands • Lipid A • Lipid Bilayers • Lipopolysaccharides • Lung • Lysine • Machado-Joseph Disease • Macromolecular Substances • Magnetic Resonance Spectroscopy • Male • Mannose • Mannose-Binding Lectins • Mannosides • Mass Spectrometry • Materials Testing • Mathematics • Matrix Metalloproteinase 3 • Matrix Metalloproteinase Inhibitors • Membrane Fusion • Membrane Potentials • Mercaptoethanol • Metabolic Networks and Pathways • Metal Nanoparticles • Metals • Methylation • Mice • Microbial Sensitivity Tests • Microscopy, Atomic Force • Microscopy, Confocal • Microscopy, Electron • Microscopy, Electron, Scanning • Microscopy, Fluorescence • Models, Biological • Models, Chemical • Models, Molecular • Models, Structural • Molecular Biology • Molecular Conformation • Molecular Sequence Data • Molecular Structure • Molecular Targeted Therapy • Monosaccharides • Muscle Contraction • Mutagenesis • Mutagenesis, Site-Directed • Mutation • Myoglobin • N-Acetylneuraminic Acid • Nanotechnology • Naphthalenes • Naphthoquinones • Neoplasms • Nerve Tissue Proteins • Neuraminidase • Neutrons • Nitric Oxide • Nitrilotriacetic Acid • Nitrites • Nitrogen • Nitrogen Oxides • Nitrosation • Nitroso Compounds • Nucleosomes • Octoxynol • Oligonucleotide Array Sequence Analysis • Oligopeptides • Oligosaccharides • Ophthalmic Solutions • Organic Chemicals • Oxidation-Reduction • Oxides • Oxygen • Peptide Library • Peptides • Permeability • Phenols • Phenotype • Phenylalanine • Phosphates • Phosphatidylcholines • Photochemistry • Photoelectron Spectroscopy • Plant Extracts • Plant Lectins • Plasmids • Polyethylene Glycols • Polymerase Chain Reaction • Polymers • Polysaccharides, Bacterial • Polyurethanes • Printing • Prodrugs • Protein Binding • Protein Conformation • Protein Engineering • Protein Folding • Protein Interaction Mapping • Protein Methyltransferases • Protein Structure, Quaternary • Protein Structure, Secondary • Protein Structure, Tertiary • Proteins • Protons • Pseudomonas aeruginosa • Pseudomonas Infections • Pyruvate Kinase • Pyruvates • Quantum Theory • Quaternary Ammonium Compounds • Quinazolines • Quinolines • Rabbits • ras Proteins • Receptor Aggregation • Receptors, Cell Surface • Recombinant Fusion Proteins • Recombinant Proteins • Repressor Proteins • Reproducibility of Results • Respiratory Function Tests • Reverse Transcriptase Polymerase Chain Reaction • S-Nitrosothiols • Salmonella • Scattering, Radiation • Semiconductors • Sequence Homology, Amino Acid • Serum Albumin • Shiga Toxin 1 • Shigella flexneri • Sialic Acids • Signal Transduction • Silicon • Silicon Compounds • Solutions • Solvents • Species Specificity • Spectrometry, Fluorescence • Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization • Spectrum Analysis • Spectrum Analysis, Raman • Stereoisomerism • Streptococcus pyogenes • Structure-Activity Relationship • Substrate Specificity • Succinates • Succinimides • Sulfhydryl Compounds • Sulfonamides • Sulfonic Acids • Sulfur • Surface Plasmon Resonance • Surface Properties • Swine • Temperature • Thermodynamics • Thermotoga maritima • Time Factors • Tin Compounds • Transcription Factors • Transcription, Genetic • Transglutaminases • Trifluoperazine • Trihexosylceramides • Trisaccharides • Tryptophan • Tyrphostins • Uridine Diphosphate Glucuronic Acid • Uridine Diphosphate Sugars • Virulence Factors • Warfarin • Water • Wnt Proteins • Zinc • Zinc Sulfate

Current Ph.D. Students   (Former Students)

  • Matthew Walters  
  • Jason King  
  • James Parise  
  • Allison Schmitt  
  • Carleen Morris  
  • Yves Wang  
  • Alexander Shestopalov  
  • Bo Choi  
  • Philip Snyder  
  • John Hatten  
  • Jennifer Griffiths  
  • Briana Vogen  
  • Daphne (Yu) Du  
  • Andrea Luteran  
  • David Carlson  
  • Corey Causey  
  • David Gooden  
Postdocs Mentored

  • Ramesh Gopalaswamy (Research Scientist) (2008/01-present)  
  • Michael Gorczynski (Research Scientist) (2008/01-present)  
  • David Gooden (Research Scientist) (2007-present)  
  • Trine Christansen (2002-2004)  
  • Steven Powell (2004)  
  • Xin Chen (Assistant Research Professor)  
Recent Publications   (More Publications)

  1. King, JR; Bowers, CM; Toone, EJ, Specific binding at the cellulose binding module-cellulose interface observed by force spectroscopy., Langmuir : the Acs Journal of Surfaces and Colloids, vol. 31 no. 11 (March, 2015), pp. 3431-3440, ISSN 0743-7463 [doi]  [abs]
  2. Sund, JB; Causey, CP; Wolter, SD; Parker, CB; Stoner, BR; Toone, EJ; Glass, JT, Diamond surface functionalization with biomimicry - Amine surface tether and thiol moiety for electrochemical sensors, Applied Surface Science, vol. 301 (May, 2014), pp. 293-299, ISSN 0169-4332 [doi]  [abs]
  3. Sund, JB; Causey, CP; Wolter, SD; Parker, CB; Stoner, BR; Toone, EJ; Glass, JT, Diamond surface functionalization with biomimicry – Amine surface tether and thiol moiety for electrochemical sensors, Applied Surface Science, vol. 301 (May, 2014), pp. 293-299, ISSN 0169-4332 [doi]
  4. Bowers, CM; Zhang, M; Lyubarskaya, Y; Toone, EJ; Tang, C; Shestopalov, AA, Structural Modifications in Bilayered Molecular Systems Lead to Predictable Changes in Their Electronic Properties, Advanced Materials Interfaces, vol. 1 no. 2 (April, 2014), pp. 1300109-1300109, ISSN 2196-7350 [doi]
  5. Xia, W; Gooden, D; Liu, L; Zhao, S; Soderblom, EJ; Toone, EJ; Beyer, WF; Walder, H; Spector, NL, Photo-activated psoralen binds the ErbB2 catalytic kinase domain, blocking ErbB2 signaling and triggering tumor cell apoptosis., Plos One, vol. 9 no. 2 (January, 2014), pp. e88983 [doi]  [abs]


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